Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.27.1 (RNase)
16,360 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The addition of detergent-solubilized influenza C virus to a reaction mixture containing ATP, CTP, GTP, [3H]UTP, and Mg2+ leads to the synthesis of an acid-insoluble, radioactive product, which is ribonuclease-sensitive. The dinucleoside monophosphate ApG clearly enhances the reaction rate, a fact which indicates that influenza C viruses follow the same strategy of transcription as influenza A and B viruses, the other members of the orthomyxovirus family.
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PMID:Influenza-C-virion-associated RNA-dependent RNA-polymerase activity. 654 51

The hemagglutinin (HA) gene of the influenza virus subtype H1N1 isolated from pigs and birds has been analyzed by the hybridization technique. According to the RNase protection data the HA genes of recent isolates from pigs in Northern Europe are genetically more closely related to those of isolates from birds in Europe and North America than to those of isolates from pigs in the United States, Taiwan, and Italy. Thus, two different H1N1 subtypes are circulating in the pig population. The results are consistent with the view that H1N1 viruses can be transmitted from birds to pigs and/or vice versa.
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PMID:Genetic relatedness of hemagglutinins of the H1 subtype of influenza A viruses isolated from swine and birds. 662 31

Ribonucleoprotein (RNP) cores with RNA-synthesizing activity were prepared in two fractions, M protein-free and M protein-associated, from detergent-treated influenza virus PR8 by centrifugation through a discontinuous triple gradient of cesium sulfate, glycerol, and NP-40. The M-free RNP was fractionated by phosphocellulose column chromatography into two major RNP forms, A and B, which differed in the content of P proteins, while the M-associated RNP gave only the low P-content Form-B RNP. Starting from the high P-content Form-A RNP, an RNA-P proteins complex virtually free from NP protein was isolated by cesium sulfate equilibrium centrifugation. The complex, containing only three P proteins (P1, P2, and P3), was still active in catalyzing RNA synthesis in vitro without addition of exogenous template, indicating that NP protein is not required for the catalysis of RNA synthesis. RNA synthesis by the isolated RNA-P proteins complex was dependent on either ApG or capped RNA primers, and required four ribonucleoside triphosphates as substrates. The RNA product in this reaction was hybridizable to viral RNA. A complex of one each of the three P proteins was separated from RNA by glycerol gradient centrifugation after ribonuclease treatment or cesium chloride equilibrium centrifugation.
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PMID:RNA polymerase of influenza virus. III. Isolation of RNA polymerase-RNA complexes from influenza virus PR8. 686 42

RNA and protein interaction in the structure of influenza virus ribonucleoprotein (RNP) was studied by ultraviolet (UV) irradiation. After UV-irradiation of virion RNP for 1 hour only 6% of 3H-uridine-labeled RNA was found to go into the aqueous phase upon phenol-detergent extraction. Pretreatment of RNP with small doses of pancreatic RNase before RNA extraction slightly increased (up to 18%) the amount of RNA going into the aqueous phase. About 90% RNA was found after extraction in the aqueous phase in the nonirradiated material. As a result of UV-irradiation of RNP, RNA in RNP became more resistant to RNase: the residual acid-insoluble radioactivity was 21% whereas with nonirradiated RNP it was 3.2%. The results of the analysis of RNP labeled for protein in polyacrylamide gel and SDS-sucrose gradient after UV-irradiation and ribonuclease treatment indicate the formation of UV-induced linkages between RNA and NP protein.
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PMID:[RNA-protein interactions in influenza virus A ribonucleoprotein detected by UV radiation]. 733 92

Influenza virus nucleoid ("core") was obtained by the treatment of virions with hydrolytic enzymes without the use of fixing agents. The "core" buoyant density in sucrose density gradient was 1.24 g/cm3. The subvirus particles are completely devoid of surface proteins, glycoproteins, and their polypeptide composition is represented by group P proteins; NP and M proteins. RNA in the core is insensitive to the effect of RNase. Morphological analysis by electron microscopy revealed the presence of spherical compact particles without spikes on their surface.
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PMID:[Preparation and investigation of some properties of influenza virus nucleoid]. 738 86

A ribonuclease activity associated with influenza virus has been purified to homogeneity. This preparation is free of DNAase, phosphodiesterase, and phosphatase activities. The purified enzyme has a pH optima of 7.0 at 37 degrees C, and moves as a single band on sodium dodecyl sulfate - polyacrylamide gel with an estimated molecular weight of 84 000.
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PMID:The isolation and properties of a ribonuclease associated with influenza virus. 738 74

By molecular hybridization and by neuraminidase inhibition tests it is shown that all influenza A strains tested carrying an Nav3 or Nav2 neuraminidase (NA) are genetically highly related in their NA genes and cross-react serologically with specific antineuraminidase sera. The Nav6 strains exhibit a very low RNase protection after hybridization and do not cross-react serologically with Nav2 or Nav3 strains. Thus, the Nav2 and Nav3 strains comprise one group which is distinct from that of Nav6 strains.
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PMID:Genetic relatedness of the neuramindase of influenza A strains Nav2, Nav3, and Nav6. 741 73

By serial subculture of MDCK cells which survived high multiplicity infections with AWBY-140, a weakly cytolytic mutant of influenza virus A/WSN (H1N1), we established a variant cell line (MDCK-L cells) that was uniquely resistant to infection with influenza A and B viruses, yielding 3 to 4 orders lower amount of progeny virus compared with MDCK cells. Competitive polymerase chain reaction revealed that the amount of primary transcript produced in MDCK-L cells infected with 10 PFU/cell of influenza virus A/Aichi was suppressed to 1/100 of that in MDCK cells similarly infected, although the amount of virus adsorbed to MDCK-L cells was 1/4 of MDCK cells. Even when MDCLK-L cells were infected with 40 PFU/cell of Aichi to overcome the lower amount of internalized virus in those cells, the results were the same. The synthesis of v-, c- and mRNAs, as well as proteins of infected A/Aichi was below detectable level in MDCK-L cells, in contrast with MDCK cells, where they were clearly demonstrable by ribonuclease protection assay or polyacrylamide gel electrophoresis.
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PMID:A variant of MDCK cell line which restricted growth of influenza viruses mainly through suppression of viral primary transcription. 867 37

We have investigated the endonuclease activity of the influenza A virus RNA polymerase in an in vitro assay with an artificial influenza-like mRNA containing a cap structure at its 5' terminus, followed by a 10 nt beta-globin mRNA sequence, and the 5' and 3' conserved termini of a truncated nucleoprotein (NP) cRNA influenza sequence. Results showed that partially purified virion ribonucleoprotein complexes (RNPs) and micrococcal nuclease treated RNPs cleaved the artificial influenza-like mRNA substrate specifically at positions near the 5' terminus to generate capped 14 and 15 nucleotide long RNA fragments which subsequently served as primers to initiate transcription. The endonuclease activity was completely blocked by addition of cap analog and competitively inhibited by added globin mRNA. Furthermore, an in vitro reconstituted influenza RNA transcription reaction containing a truncated NP vRNA as template, micrococcal nuclease treated RNPs and globin mRNA as primer, synthesized capped and uncapped full length (+) sense products. Enzyme kinetics showed that capped RNA was made earlier in the reaction; it reached a peak at 120 min and then declined. However, uncapped cRNA synthesis appeared later and remained as the dominant product later in the reaction. The nature of these products was confirmed by ribonuclease protection assays and by primer extension.
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PMID:Influenza A virus RNA-dependent RNA polymerase cleaves influenza mRNA in vitro. 880 82

A Chinese hamster alpha-tubulin cDNA was modified to encode an 11-amino acid carboxyl-terminal extension containing the immunodominant epitope from influenza hemagglutinin antigen (to create HA alpha 1-tubulin) and was cloned into a vector for expression in mammalian cells. 12 stable CHO cell lines expressing this HA alpha 1-tubulin were isolated and characterized. HA alpha 1-tubulin incorporated into all classes of microtubules, assembled to the same extent as the endogenous tubulin, and did not perturb the growth of the cells in which it was expressed. However, overexpression of HA alpha 1-tubulin strongly repressed the synthesis of endogenous alpha-tubulin while having little or no effect on the synthesis of beta-tubulin. Treatment of transfected cells with sodium butyrate to induce even greater expression of HA alpha 1-tubulin led to a further decrease in synthesis of endogenous alpha-tubulin that was fully reversible upon removal of the inducer. Decreased synthesis of alpha-tubulin in transfected cells did not result from decreased levels of alpha-tubulin mRNA, as demonstrated by ribonuclease protection assays. On the other hand, colchicine, a drug previously shown to destabilize the tubulin message, caused a clear reduction in both protein synthesis and mRNA levels for transfected HA alpha 1-tubulin and endogenous alpha-tubulin, thus indicating that the decreased alpha-tubulin synthesis observed as a result of HA alpha 1-tubulin overexpression is distinct from the previously described autoregulation of tubulin. The results are consistent with a mechanism in which free alpha-tubulin inhibits the translation of its own message as a way of ensuring stoichiometric synthesis of alpha- and beta-tubulin.
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PMID:alpha-Tubulin limits its own synthesis: evidence for a mechanism involving translational repression. 897 20


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